Issue 47, 2020

Zinc(ii) and copper(ii) complexes as tools to monitor/inhibit protein phosphorylation events

Abstract

Protein phosphorylation is a key event in the signalling pathways that control most cell functions, and its deregulation is observed in many human pathologies, including inflammatory, neurodegenerative and autoimmune diseases and cancer. Compounds able to bind phosphoproteins can potentially be used as analytical tools for investigating phosphorylation-based cell signalling and/or as inhibitors of a particular signalling pathway. Metal complexes are arguably the most important class of receptors for the recognition of phosphate-containing molecules. In the last two decades the phosphate-binding ability of metal complexes has been explored for the binding and/or sensing of phosphorylated peptides and proteins. Among those we will focus this review on mono- and dinuclear copper(II) and zinc(II) complexes of varied ligand architectures used as binders of phosphorylated peptides and proteins and as sensors of phosphorylation reactions with fluorescence or other techniques in real-time. The cumulative information of strong and selective associations of the indicated receptors allowed selecting some of them for phosphoprotein/peptide enrichment and staining procedures, in vitro monitoring of kinase/phosphatase activity and disruption of phosphorylation-dependent protein–protein interactions. A perspective on the advance of this important area on the frontier between chemistry and biology is presented.

Graphical abstract: Zinc(ii) and copper(ii) complexes as tools to monitor/inhibit protein phosphorylation events

Article information

Article type
Perspective
Submitted
09 okt 2020
Accepted
02 nov 2020
First published
04 nov 2020

Dalton Trans., 2020,49, 17076-17092

Zinc(II) and copper(II) complexes as tools to monitor/inhibit protein phosphorylation events

P. Mateus and R. Delgado, Dalton Trans., 2020, 49, 17076 DOI: 10.1039/D0DT03503C

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements